Structure of PDB 5lr8 Chain B

Receptor sequence
>5lr8B (length=843) Species: 112509 (Hordeum vulgare subsp. vulgare) [Search protein sequence]
IDSSAIASNIQHHADFTPLFSPEHSSPLKAYHATAKSVFDSLIMNWNATY
DYYNKVNAKQAYYLSMEFLQGRALTNAIGNLELTGQYAEALKQLGHNLED
VASQEPDPALGNGGLGRLASCFLDSLATLNYPAWGYGLRYRYGLFKQIIT
KDGQEEVAENWLEMGNPWEIVRNDVSYPVKFYGKVVEGTDGRKHWIGGEN
IKAVAHDVPIPGYKTKTTNNLRLWSTTVPSQNFDLGAFNAGDHAKANEAH
LNAEKICHVLYPGDESSEGKILRLKQQYTLCSASLQDIISRFESRAGDSL
NWEDFPSKVAVQMNDTHPTLCIPELMRILMDIKGLSWNEAWSITERTVAY
TNHTVLPEALEKWSLDIMQKLLPRHVEIIETIDEELMNNIVSKYGTADIS
LLKQKLKDMRILDNVDLPASVAKLFIKELDPFAKYDPQFPRVVRMANLCV
VGGHSVNGVAEIHSEIVKQDVFNSFYEMWPTKFQNKTNGVTPRRWIRFCN
PELSTIISKWIGSDDWILNTDKLAGLKKFADDEDLQSEWRTAKRNNKMKV
VSLIRDKTGYIVSPDAMFDVQVKRIHEYKRQLLNILGIVYRYKKMKEMSA
KDRRKSFVPRVCIFGGKAFATYVQAKRIVKFITDVAATVNYDPDIGDLLK
VVFVPDYNVSVAETLIPASELSQHISTAGMEASGTSNMKFAMNGCLLIGT
LDGANVEIREEVGEENFFLFGAHAPEIAGLRQERAEGKFVPDLRFEEVKE
YVRSGVFGTSNYDELMGSLEGNEGYGRADYFLVGKDFPSYIECQEKVDEA
YRDQKLWTRMSILNTAGSPKFSSDRTIHEYAKDIWDISPVIMP
3D structure
PDB5lr8 Functional and structural characterization of plastidic starch phosphorylase during barley endosperm development.
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H421 K698 R699 K704 T810 K814
Catalytic site (residue number reindexed from 1) H353 K573 R574 K579 T685 K689
Enzyme Commision number 2.4.1.1: glycogen phosphorylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PLP B L137 G182 W620 Y782 N783 V784 T810 S811 K814 L69 G114 W495 Y657 N658 V659 T685 S686 K689
Gene Ontology
Molecular Function
GO:0004645 1,4-alpha-oligoglucan phosphorylase activity
GO:0008184 glycogen phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009266 response to temperature stimulus
GO:0009414 response to water deprivation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5lr8, PDBe:5lr8, PDBj:5lr8
PDBsum5lr8
PubMed28407006
UniProtF2E0G2

[Back to BioLiP]